Histone 2B can be modified by the attachment of ubiquitin.
about
WAC, a functional partner of RNF20/40, regulates histone H2B ubiquitination and gene transcriptionCharacterization of E3Histone, a novel testis ubiquitin protein ligase which ubiquitinates histones.Ubiquitin-specific proteases 7 and 11 modulate Polycomb regulation of the INK4a tumour suppressorUbiquitin is covalently attached to the p6Gag proteins of human immunodeficiency virus type 1 and simian immunodeficiency virus and to the p12Gag protein of Moloney murine leukemia virusRetroviruses have differing requirements for proteasome function in the budding processNp95 is a histone-binding protein endowed with ubiquitin ligase activityDynamic regulation and function of histone monoubiquitination in plantsPredominant occupation of the class I MHC molecule H-2Kwm7 with a single self-peptide suggests a mechanism for its diabetes-protective effect.Rad6 plays a role in transcriptional activation through ubiquitylation of histone H2B.Direct Bre1-Paf1 complex interactions and RING finger-independent Bre1-Rad6 interactions mediate histone H2B ubiquitylation in yeastHistone ubiquitylation and its roles in transcription and DNA damage responseHistone ubiquitination: a tagging tail unfolds?The ubiquitin-conjugating DNA repair enzyme HR6A is a maternal factor essential for early embryonic development in mice.RNF8-dependent histone modifications regulate nucleosome removal during spermatogenesisStructural mechanism for the recognition and ubiquitination of a single nucleosome residue by Rad6-Bre1Application of the protein semisynthesis strategy to the generation of modified chromatinAntibacterial peptides in stimulated human granulocytes: characterization of ubiquitinated histone H1A.Ubiquitin is a component of the microtubule networkUbiquitin is associated with abnormal cytoplasmic filaments characteristic of neurodegenerative diseases.Histone acetylation: influence on transcription, nucleosome mobility and positioning, and linker histone-dependent transcriptional repression.The structure of ubiquitinated histone H2B.The polyubiquitin Ubc gene modulates histone H2A monoubiquitylation in the R6/2 mouse model of Huntington's disease.The role of deubiquitinating enzymes in chromatin regulation.A specific endpoint assay for ubiquitinUbiquitin has intrinsic proteolytic activity: implications for cellular regulation.Histone H2B ubiquitylation disrupts local and higher-order chromatin compaction.RNF8-dependent histone ubiquitination during DNA damage response and spermatogenesisDetection and characterization of ubiquitylated H2B in mammalian cells.Altered testicular gene expression patterns in mice lacking the polyubiquitin gene UbbSelective presence of ubiquitin in intracellular inclusions.Histone H2B ubiquitylation and H3 lysine 4 methylation prevent ectopic silencing of euchromatic loci important for the cellular response to heat.Histone H2B ubiquitination and beyond: Regulation of nucleosome stability, chromatin dynamics and the trans-histone H3 methylation.The active immunoglobulin kappa chain gene is packaged by non-ubiquitin-conjugated nucleosomes.Remodeling somatic nuclei in Xenopus laevis egg extracts: molecular mechanisms for the selective release of histones H1 and H1(0) from chromatin and the acquisition of transcriptional competence.Histone ubiquitination and deubiquitination in transcription, DNA damage response, and cancer.Histone deacetylase inhibitors: clinical implications for hematological malignancies.Histone modifications in Trypanosoma bruceiHistone monoubiquitylation position determines specificity and direction of enzymatic cross-talk with histone methyltransferases Dot1L and PRC2.Differential conservation of histone 2A variants between mammals and sea urchins.A 17-kD centromere protein (CENP-A) copurifies with nucleosome core particles and with histones.
P2860
Q24293427-864D364D-F2AD-47F0-B879-D28E3F2B944FQ24298059-DFDA1645-81FE-4CC7-9A09-FC88419F700AQ24337508-111865F4-2293-43C5-AE8E-F8D9EE403359Q24523226-C24FCB0D-31AF-4ABB-839E-3469750E1DF8Q24550599-0A81AD9C-616B-43A1-B895-FC8C2646F5C4Q24629660-5ED8E6AF-2CEB-45C9-B6E1-25C5E5D2E646Q26830273-F2F39DE9-2F33-4FBE-BE1D-BA3EB1233C85Q27659105-7085FE64-7FC1-486F-B094-A415CA217FA6Q27930655-7A11AB2F-188E-4401-90B0-0449FC35C457Q27936986-5A9C07E8-7B44-4904-8B52-5383FEFA8D43Q28081194-31CD72A4-A65F-45E4-85F9-EFB376B6AC6CQ28218018-D73C571B-528B-4E3D-A849-AD21C2F68310Q28587712-0665D2F4-BCA0-47D6-A990-C5130144B30EQ28589254-6CDF858E-7B42-40B0-B175-59D4F237A9FCQ28829129-CD97213C-B5A6-4B71-A521-7E24369450F6Q28831322-8268F761-ADBC-4842-B149-6F063AF50585Q31039333-30D3D175-5C01-4370-8A1F-4E036B9E738CQ33570095-2570CAC9-9089-439B-932E-BE62B9F10FEDQ33582814-2380F95D-5A16-4A79-943C-9B78A834D08FQ33886463-DD2B9559-5BDF-4E27-B353-E5574FF69F18Q33929065-24616C3B-7C08-465C-B537-C9F20D94379CQ33942346-8F4448D9-C1EB-4BF5-84D2-A2ACE676BC80Q34564968-2D2C6E68-1A19-4D89-8A84-272C305C7956Q34603909-95B560EB-DEC0-4933-9887-C22D48EFBFECQ34627204-B3B7539D-F3F6-459B-BA60-2EBE87A8B733Q34808188-B9A364F1-21A1-4B77-98D4-6641F477CFE6Q34829400-437D0077-F434-4148-9D40-3C45DBBEF404Q35056503-063E6188-0D38-4A26-84E6-E3FD7498C147Q35097653-82CEC3A9-859F-4BC6-A3D5-3BCAD8092E94Q35130070-BF4058A9-C05A-4A34-9825-D0B5A732AB95Q35133622-2E2D0636-286A-4FA3-B623-472743C024F1Q35592200-10B036AE-8D5F-4CBC-B920-C2544A6C23AFQ35607749-E6ED1750-CE15-44F9-AC72-2CE58EDB1EF8Q35912329-F593C7C3-0D7A-410A-8C20-F8CAF8902D1FQ35971184-F3C01C36-1C06-451C-B668-6C38160036FFQ36001847-55BD4BA8-A0F7-412D-AF5D-96A0E8DFDF50Q36050647-5BFC25CA-C403-469E-95E4-486B734C4B80Q36078818-AF32AC9E-B064-4D91-BC52-264FA2D1D789Q36208916-28412D02-C06C-440B-83B2-C17B757B5D37Q36215978-DB84FD21-EC17-4828-BC83-E7F0EEAC3D29
P2860
Histone 2B can be modified by the attachment of ubiquitin.
description
1980 nî lūn-bûn
@nan
1980年の論文
@ja
1980年論文
@yue
1980年論文
@zh-hant
1980年論文
@zh-hk
1980年論文
@zh-mo
1980年論文
@zh-tw
1980年论文
@wuu
1980年论文
@zh
1980年论文
@zh-cn
name
Histone 2B can be modified by the attachment of ubiquitin.
@ast
Histone 2B can be modified by the attachment of ubiquitin.
@en
type
label
Histone 2B can be modified by the attachment of ubiquitin.
@ast
Histone 2B can be modified by the attachment of ubiquitin.
@en
prefLabel
Histone 2B can be modified by the attachment of ubiquitin.
@ast
Histone 2B can be modified by the attachment of ubiquitin.
@en
P356
P1476
Histone 2B can be modified by the attachment of ubiquitin.
@en
P2093
P304
P356
10.1093/NAR/8.20.4671
P407
P577
1980-10-01T00:00:00Z